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1gll

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==About this Structure==
==About this Structure==
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1GLL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GLL OCA].
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1GLL is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GLL OCA].
==Reference==
==Reference==
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Crystal structures of Escherichia coli glycerol kinase variant S58-->W in complex with nonhydrolyzable ATP analogues reveal a putative active conformation of the enzyme as a result of domain motion., Bystrom CE, Pettigrew DW, Branchaud BP, O'Brien P, Remington SJ, Biochemistry. 1999 Mar 23;38(12):3508-18. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10090737 10090737]
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<ref group="xtra">PMID:10090737</ref><references group="xtra"/>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Glycerol kinase]]
[[Category: Glycerol kinase]]
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[[Category: Single protein]]
 
[[Category: Branchaud, B P.]]
[[Category: Branchaud, B P.]]
[[Category: Bystrom, C E.]]
[[Category: Bystrom, C E.]]
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[[Category: Phosphotransferase]]
[[Category: Phosphotransferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 05:29:05 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 07:02:26 2009''

Revision as of 05:02, 18 February 2009

Image:1gll.png

Template:STRUCTURE 1gll

ESCHERICHIA COLI GLYCEROL KINASE MUTANT WITH BOUND ATP ANALOG SHOWING SUBSTANTIAL DOMAIN MOTION

Template:ABSTRACT PUBMED 10090737

About this Structure

1GLL is a 2 chains structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

Reference

  • Bystrom CE, Pettigrew DW, Branchaud BP, O'Brien P, Remington SJ. Crystal structures of Escherichia coli glycerol kinase variant S58-->W in complex with nonhydrolyzable ATP analogues reveal a putative active conformation of the enzyme as a result of domain motion. Biochemistry. 1999 Mar 23;38(12):3508-18. PMID:10090737 doi:10.1021/bi982460z

Page seeded by OCA on Wed Feb 18 07:02:26 2009

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